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PubMed1987

Absorption of protein via the intestinal wall. A quantitative model.

Intact, biological active insulin and pancreatic RNase can be absorbed from the intestinal lumen into the blood circulation. The absorption is dependent on the addition of bile acid (sodium cholate) and proteinase inhibitor. The quantitative absorption of insulin and pancreatic RNase has been demonstrated in an in situ model. The amount of insulin absorbed after 30 min from the ileum to the mesenteric vein was 0.025% of the initial amount. Sodium cholate (10 mg/ml) and 3000 KIU/ml aprotinin enhanced this absorption by 30 times. The amount of pancreatic RNase which was absorbed from the ileum to the blood was 0.002% of the initial amount during 30 min. Sodium cholate (10 mg/ml) and 3000 KIU/ml aprotinin increased the absorption by a factor of 200. No damage occurred to the intestine during the experimental procedures. The sieving characteristics of the intestinal wall were not altered by the presence of sodium cholate and proteinase inhibitor in the intestinal lumen. These results suggest that sodium cholate and proteinase inhibitors can facilitate the absorption of intact, biologically active proteins across the intestinal wall.

Animals↗

PubMed1987

Purification and characterization of murine protoporphyrinogen oxidase.

The penultimate enzyme of the heme biosynthetic pathway, protoporphyrinogen oxidase (EC 1.3.3.4), has been purified to apparent homogeneity from mouse liver mitochondria. The purification involves solubilization from mitochondrial membranes with sodium cholate followed by ammonium sulfate fractionation and gel filtration on a Sepharose CL-6B column. The eluate is adjusted to 0.67 M (NH4)2SO4 and loaded onto a phenyl-Sepharose column. After salt washes, the enzyme is eluted with 0.5% sodium cholate and 0.5% Brij 35. The final step is high-pressure ion-exchange chromatography on a DEAE-5PW column. The purified protein has a molecular weight of approximately 65,000 by gel filtration chromatography on Sepharose CL-6B in the presence of 0.5% sodium cholate. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis shows a single band corresponding to a molecular weight of 65,000. The absorption spectrum of the purified enzyme shows no evidence of a chromophoric cofactor. Purified protoporphyrinogen oxidase has a Km for protoporphyrinogen IX of 5.6 microM with a Vmax of 2300 nmol mg-1 h-1. It utilizes meso- and hematoporphyrinogen at about 10% the level of protoporphyrinogen. The pH optimum is broad with a maximum at 7.1. There is no stimulation or inhibition by any tested divalent cations, and sulfhydryl reagents have no inhibitory effect on the purified enzyme.

Animals↗

PubMed1982

Distribution of bile salts between 1-octanol and aqueous buffer.

The distribution of four bile salts: sodium cholate (I), sodium deoxycholate (II), sodium chenodeoxycholate (III), and sodium ursodeoxycholate (IV), between aqueous buffer and 1-octanol has been measured as a function of temperature between 25 and 55 degrees and as a function of bile salt concentration at concentrations less than 0.1 mole/liter in the aqueous phase. The distribution isotherms obtained have been explained on the basis of reversible association in the aqueous phase. The treatment assumes that the bile acid exists as a monomer in the organic phase, which is verified by vapor pressure osmometry. A graphical method has been employed to estimate the association constants in the aqueous phase for the various equilibria encountered. An aggregation number of four for IV and 12 for I, II, and III has been estimated. From the results, thermodynamic functions associated with the transfer of each of the bile salts from water to octanol and those associated with association processes in the aqueous phase were calculated. These results are consistent with previous findings that the premicellar association of bile salts occurs by hydrophobic interaction. The thermodynamics of transfer of bile salts revealed an unfavorable enthalpic and favorable entropic contribution for all four bile salts. However, for IV, which is an epimer of III, both enthalpic and entropic contributions are reduced, compared to III, suggesting a pronounced effect of stereochemical orientation on hydrophobic interaction.

1-Octanol↗

PubMed1983

Effects of surfactants on the GI absorption of beta-lactam antibiotics in rats.

The effects of various nonionic and ionic surfactants and two bile salts (sodium cholate and sodium taurocholate) on the GI absorption of beta-lactam antibiotics were investigated using the in situ rat GI perfusion technique. Addition of 10 mM polyoxyethylene-23-lauryl ether in the perfusion solution reduced the absorption of propicillin by the stomach and markedly increased the absorption of propicillin and cefazolin by the small intestine. Ester-type nonionic surfactants and bile salts exerted no significant influence on the intestinal absorption of these antibiotics.

Animals↗

PubMed1991

Increasing the in vitro bile acid binding capacity of diethylaminoethylcellulose by quaternization.

Diethylaminoethylcellulose (DEAE-cellulose) was quaternized with methyl iodide (DEAE-cellulose-CH3I), and its in vitro binding capacity for sodium glycocholate, at room temperature, in water, Tris-HCl buffer (0.0015-0.0050 M, pH 7.0), and aqueous NaCl (0.0025 M) was determined by reversed-phase HPLC. Quaternization increased the in vitro bile salt binding capacity of DEAE-cellulose. On a molar basis, the binding capacity was greater than that of cholestyramine, a cholesterol-lowering agent. Increasing the ionic strength of the medium decreased the binding capacities, as expected if ionic interactions are important. However, conversion of DEAE-cellulose-CH3I to its chloride form did not change the binding capacity. The bile salt binding capacity of DEAE-cellulose-CH3I was similar for both sodium cholate and sodium glycocholate.

Adsorption↗

PubMed2005

Micellar electrokinetic chromatography for simultaneous determination of six corticosteroids in commercial pharmaceuticals.

We have developed a micellar electrokinetic chromatography (MEKC) method using bile salts for the simultaneous determination of six corticosteroids, including betamethasone, cortisone, prednisolone, 6alpha-methylprednisolone, triamcinolone, and prednisone. The separation was performed using borate buffer containing sodium cholate and sodium deoxycholate. Several parameters were studied, including bile salt concentrations, concentrations and pH of borate buffer, and analytical voltages. In method validation, calibration curves were linear over a range of 10-100 microM for each corticosteroid. The RSD (relative standard deviation) and RE (relative error) were all less than 5% for intra- and interday assays. The limit of detection of each analyte was 5 microM. The recoveries were greater than 95%. Application of this method for quality control of commercial tablets also proved to be feasible. All analytical values fall within the labeled amount of 90-110% for betamethasone and prednisolone, and of the labeled amount of 92.5-107.5% for 6alpha-methylprednisolone, as required by the United State Pharmacopeia 25 (USP 25).

Adrenal Cortex Hormones↗

PubMed2007

Proton NMR assignments for R,S-1,1'-binaphthol (BN) and R,S-1,1'-binaphthyl-2,2'-diyl hydrogen phosphate (BNDHP) interacting with bile salt micelles.

We report proton chemical shifts for two model chiral analytes that are commonly used in the study of micellar electrokinetic capillary chromatography (MEKC), R,S-1,1'-binaphthol (1, BN) and R,S-1,1'-binaphthyl-2,2'-diyl hydrogen phosphate (2, BNDHP), in the absence and presence of monomers and micelles of sodium cholate and sodium deoxycholate. The analytes undergo fast exchange in and out of the micelles, which perturbs the analytes' chemical shifts, and which we use to resolve some resonances that are degenerate at both 300 and 600 MHz. Although BN and BNDHP are simple molecules, the proton assignments are only unambiguously established with the aid of the exchange with micelles, an attractive alternative to other methodologies such as the use of paramagnetic shift reagents which may also cause spectral distortions. We rely also upon 2D-NOE spectra of samples in the presence of micelles to perform these assignments. Recently published assignments, which were based upon 2D-COSY spectroscopy, appear to be in error and are corrected here. Finally, we note that these shifts are information-rich reporters on the nature of the interactions of these model analytes with the micelles.

Journal Article↗

PubMed2003

Proteomic analysis of the cell envelope fraction of Escherichia coli.

We applied proteomics technologies to analyze a membrane preparation of Escherichia coli, wild type strain and of transformants expressing human cytochrome P450s. The proteins were analyzed by two-dimensional electrophoresis and identified by matrix-assisted laser desorption ionization mass spectrometry. The membrane proteins were solubilized with both mild detergents such as CHAPS and strong detergents, such as sodium and lithium dodecyl sulfate, sodium cholate and sodium deoxycholate. In the E. colimembrane fraction, 394 different gene products were identified. Approximately 28% of them were predicted to be integral membrane proteins, of which 100 proteins have been predicted to carry one transmembrane region, ten proteins to carry two, and two proteins to include three transmembrane domains. The remaining are probably membrane-associated and cytosolic proteins. Cytochrome P450s did not enter the immobilized pH gradient strips but were efficiently analyzed in a two-dimensional, two-detergent system. Use of strong solubilizing agents resulted in the detection of about 20 membrane proteins, which were not detected following extraction with mild detergents and chaotropes. The present database is one of the largest for membrane proteins.

Electrophoresis, Gel, Two-Dimensional↗

PubMed1983

Bile salts facilitate the absorption of heparin from the intestine.

Heparin was absorbed through the rectal mucosa of rodents and primates only when administered in solutions containing sodium cholate or sodium deoxycholate (DOC). The absorption of heparin was monitored by following the increase in plasma radioactivity after administration of [35S]heparin, and by measurement of its biological effects: plasma lipase activity and prolongation of partial thromboplastin time (PTT). Following administration of the same concn of heparin in solutions lacking bile salts, there was almost no radioactivity in the blood, no prolongation of PTT and no release of plasma lipase activity. The PTT effect was found to be a less sensitive test of heparin absorption than the plasma lipase activity.

Animals↗

PubMed1992

Effect of benzimidazole drugs on the uptake of low molecular weight nutrients in Trichuris globulosa.

Thiabendazole (100 microM) and fenbendazole (250 microM) were found to inhibit U-14 C-glucose, (Na)-1-14C-palmitate and (Na)-1-14 C-acetate uptake markedly (P less than 0.001) in adult Trichuris globulosa. The inhibition was more pronounced with thiabendazole than with fenbendazole. 14C-Glucose was found to be Na(+)-dependent and a mediated process. Bile salts, viz. sodium cholate and sodium desoxycholate in the concentration range of 5-10 mM, were found to inhibit the uptake of 14C-glucose and 14C-palmitate (P less than 0.01) by the parasites. The optimum pH for (Na)-1-14C-palmitate and (Na)-1-14C-acetate uptake was 6.7 and 6.2, respectively while the optimum temperature for the uptake of these compounds was 37 degrees C.

Acetates↗

PubMed1996

Effects of bile salt structure on chiral separations with mixed micelles of bile salts and polyoxyethylene ethers using micellar electrokinetic capillary chromatography.

The chiral resolving abilities of micellar solutions of four different bile salts alone and in mixtures with polyoxyethylene-4-dodecyl ether (C12E4) and methanol were investigated using MECC. The four bile salts investigated were the unconjugated sodium salts of cholic, deoxycholic, chenodeoxycholic and ursodeoxycholic acids. The test solutes included verapamil, norverapamil, gallopamil, bi-2-naphthol, atenolol and BAYK8644. The relative hydrophobicities of the micellar aggregates formed in solutions of binary mixtures of each bile salt with C12E4 were investigated by fluorescence spectroscopy using pyrene as a probe molecule. The observed enantiomeric resolution for the test compounds using these binary mixtures as MECC pseudo-stationary phases was determined. Correlations between micellar hydrophobicity for these solutions and chiral resolution of these test solutes are presented. The addition of C12E4 with or without methanol to solutions of sodium cholate and sodium deoxycholate enhanced the chiral resolution observed for compounds containing a longer hydrocarbon chain separating some of the major functional groups from the chiral center. The pure bile salt solutions generally provided better chiral resolution for the compounds where the major functional groups, such as aromatic rings, were closer to the chiral center.

Bile Acids and Salts↗

PubMed2005

Cholesterol-bile salt vesicles as potential delivery vehicles for drug and vaccine delivery.

The aim of this study was to further investigate the interactions between cholesterol (CH) and mixed bile salts (BS) (sodium cholate and sodium deoxycholate) and their suitability for drug and vaccine delivery. Insulin was used as a model protein to assess the ability of CH:BS vesicles to entrap a therapeutically relevant macromolecule. The association of protein (FITC-insulin) with the CH:BS structure was confirmed with fluorescence microscopy, and the overall morphology of the vesicles was examined with atomic force microscopy (AFM). Results demonstrate that the nature of the vesicles formed between CH and BS is dependent not only on the concentration of BS but also on the increasing CH concentration leading to CH crystal formation.

Bile Acids and Salts↗

PubMed2005

Physicochemical studies on microemulsions 9. Conductance percolation of AOT-derived W/O microemulsion with aliphatic and aromatic hydrocarbon oils.

Both volume- and temperature-induced percolation of conductance of w/o microemulsions formed with AOT in cyclic aliphatic and aromatic oils (cyclohexane, cyclohexanone, toluene, and xylenes), and volume percolation of water/AOT/oil systems using linear aliphatic hydrocarbons (n-hexane, n-heptane, n-octane, i-octane, and n-decane) have been studied. The effect of additives, viz. sodium cholate (NaC), sodium deoxycholate (NaDC), cholesterol, n-butanol, and t-butanol, toluene, and xylenes (o, m, and p) on the temperature-induced percolating processes using the oils cyclohexane and cyclohexanone has been examined. The percolation results have been analyzed in the light of scaling equation, and the energy of activation of the ion-transport phenomenon has been evaluated for both pre- and postpercolation stages. From the percolation data, the diameter of the microdispersed water droplets, their population, and surface area have been estimated. The enthalpy of dispersion of water in AOT/oil medium has been determined from isothermal titration calorimetric (ITC) measurements.

Journal Article↗

PubMed2005

FT-IR spectroscopic study on the variations of molecular structures of some carboxyl acids induced by free electron laser.

Free electron laser has been developed as tunable lasers over a wide range of wavelengths. Devices irradiating in the region of 6-16 microm (1666-625 cm-1) are operable in the Beijing free electron lasers facilities (BFEL). For understanding the interactions between FEL and biological tissues, in this study wavelength-selective infrared-induced structure changes of substances under irradiation by FEL were measured using FT-IR spectroscopy. The carboxyl acids and carboxylates samples investigated include salicylic acid, sulfosalicylic acid, cholic acid, deoxycholic acid, sodium cholate and sodium deoxycholate. The changes of the FT-IR spectra of the molecules prove that the spectral variations of the samples induced by FEL are closely related to their hydrogen bond networks.

Carboxylic Acids↗

PubMed1998

Increasing drug solubility by means of bile salt-phosphatidylcholine-based mixed micelles.

Study of the solubilization of commercial grades of soya phosphatidylcholine (SPC) with different purities by bile salts (BS) indicated that only highly pure grades of SPC are suitable for the preparation of clear solutions of BS/SPC-mixed micelles (BS/SPC-MM). The solubilizing capacity of different BS towards SPC increased in the following order; Sodium cholate (SC) < sodium deoxycholate (SDC) < sodium glycocholate (SGC). Moreover, egg phosphatidylcholine (EPC) was solubilized to a higher extent than SPC. Furthermore, the solubility study of different drugs in the prepared MM showed substantial enhancement of solubility, the extent of which is essentially affected by the chemical nature of the drug and the composition of MM. Benzodiazepine drugs such as clonazepam, tetrazepam, diazepam, and lorazepam displayed higher affinity for MM compared with BS alone, whereas steroidal drugs, such as estradiol, prednisolone and progesterone, compared with benzodiazepines, displayed relatively higher affinity for BS alone. The solubilizing capacity of MM for the different drugs was increased to different degrees by the addition of benzyl alcohol which was comparable to the solubility of the drug in pure benzyl alcohol. The interaction between benzyl alcohol and the drug in MM could be proved by NMR.

Benzyl Alcohol↗

PubMed1998

Mimicking initial interactions of bacteriophage M13 coat protein disassembly in model membrane systems.

The structure and changes in environment of the M13 major coat protein were studied in model systems, mimicking the initial molecular process of the phage disassembly. For this purpose we have systematically studied protein associations with various detergents and lipids in two different coat protein assemblies: phage particles and S-forms. It is remarkable that the major coat protein can change its conformation to accommodate three distinctly different environments: phage filament, S-form, and membrane-bound form. The structural and environmental changes during this protein transformations were studied by site-directed spin labeling, fluorescence labeling, and CD spectroscopy in different membrane model systems. The phage particles were disrupted only by strong ionic detergents [sodium dodecyl sulfate (SDS) and cetyltrimethylammonium bromide and (CTAB)] but were not affected by sodium cholate and sodium deoxycholate, nonionic detergents, and dilauroyl-l-alpha-phosphatidylcholine (DLPC) lipid bilayers. Conversion of the phage particles into S-forms by addition of chloroform rendered the coat protein accessible for the association with different ionic and nonionic detergents, as well as DLPC lipids. The disruption of the S-form by all detergents studied was instantaneous but was slower with DLPC vesicles. Only small unilamellar vesicles effectively solubilized the S-form. The data suggest that the viral protein coat is inherently unstable when the major coat protein is exposed to amphiphilic molecules. During conversion from the phage to the S-form, and subsequently to the membrane-bound form, the coat protein undergoes pronounced changes in environment, and in response the alpha-helix content decreases and the local protein structure changes dramatically. This adaptation of the protein conformation enables a stable association of the protein with the membrane.

Bacteriophage M13↗

PubMed2005

Molecular recognition thermodynamics of bile salts by beta-cyclodextrin dimers: Factors governing the cooperative binding of cyclodextrin dimers.

The complex stability constants (K(S)), standard molar enthalpy (DeltaH degrees), and entropy changes (DeltaS degrees) for the inclusion complexation of two families of beta-cyclodextrin (beta-CD) dimers, i.e. beta-CD dimers Se1-Se4 bearing 2,2'-diselenobis(benzoyl) tether (Se-dimers) and beta-CD dimers Py1-Py4 bearing 2,2'-bipyridine-4,4'-dicarboxy tether (Py-dimers), with four bile salt guests, i.e. sodium cholate (CA), sodium deoxycholate (DCA), sodium glycocholate (GCA), and sodium taurocholate (TCA), were determined at 25 degrees C in Tris buffer solution (pH 7.4) at 298.15 K by means of isothermal titration microcalorimetry. The thermodynamic parameters obtained, together with the ROESY spectra of interactions between beta-CD dimers and bile salts, consistently suggest that the length, flexibility, and structure of spacers linking the two beta-CD cavities not only determine the binding modes but also significantly alter the molecular selectivity of beta-CD dimers.

Calorimetry↗

PubMed1978

Adsorption of bile salts from aqueous solution by plant fibre and cholestyramine.

1. Adsorption of bile salts by dietary fibre is believed to promote their excretion and hence to reduce the serum cholesterol level in man and experimental animals. 2. We have tested a number of plant fibre fractions and other related materials for their ability to adsorb bile salts from aqueous solution. The "insoluble" plant fractions were from "dry grain" (a residue from brewing), apple, wheat bran, lucerne (Medicago sativa), soya beans, mung beans (Phaseolus mungo), chick peas (Cicer arietinum), rolled oats, spinach (Spinacia oleracea), sunflower seeds, sawdust and sheep faeces. The other materials were cholestyramine, pectin and lignins prepared from wheat bran and from sawdust. 3. Only cholestyramine and the fibre from lucerne, soya beans, mung beans, chick peas, spinach, and sunflower seeds adsorbed enough of either sodium cholate or sodium deoxycholate for adsorption to be detectable. 4. This result conflicts with a report that the lignin component of dietary fibre is responsible for adsorption of bile salts. 5. Adsorption of bile salts, when it occurs, may depend on the presence of saponins bound to the fibre.

Adsorption↗